Relationship between pyridinoline concentration and thermal stability of bovine intramuscular collagen

• Published in: Journal of animal science Vol. 69; no. 5; p. 1989
• Main Authors: Smith, S.H. (Purdue University, West Lafayette, IN), Judge, M.D
• Format: Journal Article
• Language: English
• Published: United States 01.05.1991
• Subjects: AGE; Amino Acids - analysis; Animals; CALOR; Calorimetry, Differential Scanning; CARNE DE RES; Cattle; CHALEUR; COLAGENOS; Collagen - chemistry; Collagen - isolation & purification; COLLAGENE; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; Drug Stability; EDAD; Hot Temperature; MADUREZ; MATURITE; Meat - standards; MERMA; Muscles; PROPIEDADES TERMICAS; PROPRIETE THERMIQUE; RESISTANCE A LA TEMPERATURE; RESISTENCIA A LA TEMPERATURA; RETRAIT; Solubility; TEMPERATURA; TEMPERATURE; VIANDE BOVINE
• ISSN: 0021-8812; 1525-3163
• DOI: 10.2527/1991.6951989x

Semimembranosus muscle samples were obtained from 49 Holstein beef animals representing different USDA maturities. Intramuscular collagen (IMC) was isolated in the frozen state and evaluated for heat-labile collagen solubility (% Sol), thermal shrinkage temperature (Ts), enthalpy (Hs) changes, and mature crosslink (pyridinoline) content. These measures were obtained to elucidate a relationship between pyridinoline content of IMC and beef maturity level and to relate IMC thermal stability (% Sol, Ts, and Hs) to pyridinoline content. With increasing maturity, % Sol decreased (P 01) and Ts, increased (P 01), whereas Hs showed no change (P 05). Thus, IMC melted at increasing temperatures, but the amount of energy required to induce this endothermic change remained constant throughout maturation. The pyridinoline content of IMC increased (P 01) linearly with maturity, indicating that this heat-stable, mature crosslink enhances thermal stability of IMC as beef muscle matures. Significant correlations between pyridinoline content and maturity (r